@article{open236,
          volume = {12},
          number = {9},
           month = {September},
          author = {Jyoti Sarin and G.P.S. Raghava and Pradip K Chakraborti},
            note = {Copyright of this article belongs to Wiley.
Supplemental material: See www.proteinscience.org.},
           title = {Intrinsic contributions of polar amino acid residues toward thermal stability of an ABC-ATPase of mesophilic origin.},
       publisher = {Wiley},
            year = {2003},
         journal = {Protein science : a publication of the Protein Society},
           pages = {2118--20},
        keywords = {ATP-binding cassette ATPase; polar amino acid; PstB; thermostability},
             url = {http://crdd.osdd.net/open/236/},
        abstract = {The nucleotide-binding subunit of phosphate-specific transporter (PstB) from mesophilic bacterium, Mycobacterium tuberculosis, is a unique ATP-binding cassette (ABC) ATPase because of its unusual ability to hydrolyze ATP at high temperature. In an attempt to define the basis of thermostability, we took a theoretical approach and compared amino acid composition of this protein to that of other PstBs from available bacterial genomes. Interestingly, based on the content of polar amino acids, this protein clustered with the thermophiles.}
}